Costimulation of T-Cell Activation and Virus Production by B7 Antigen on Activated CD4+ T Cells from Human Immunodeficiency Virus Type 1-Infected Donors OMAR K

Copy Link

Recommended publications

Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse

Welcome to More Choice CD Marker Handbook For more information, please visit: Human bdbiosciences.com/eu/go/humancdmarkers Mouse bdbiosciences.com/eu/go/mousecdmarkers Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse CD3 CD3 CD (cluster of differentiation) molecules are cell surface markers T Cell CD4 CD4 useful for the identification and characterization of leukocytes. The CD CD8 CD8 nomenclature was developed and is maintained through the HLDA (Human Leukocyte Differentiation Antigens) workshop started in 1982. CD45R/B220 CD19 CD19 The goal is to provide standardization of monoclonal antibodies to B Cell CD20 CD22 (B cell activation marker) human antigens across laboratories. To characterize or “workshop” the antibodies, multiple laboratories carry out blind analyses of antibodies. These results independently validate antibody specificity. CD11c CD11c Dendritic Cell CD123 CD123 While the CD nomenclature has been developed for use with human antigens, it is applied to corresponding mouse antigens as well as antigens from other species. However, the mouse and other species NK Cell CD56 CD335 (NKp46) antibodies are not tested by HLDA. Human CD markers were reviewed by the HLDA. New CD markers Stem Cell/ CD34 CD34 were established at the HLDA9 meeting held in Barcelona in 2010. For Precursor hematopoetic stem cell only hematopoetic stem cell only additional information and CD markers please visit www.hcdm.org. Macrophage/ CD14 CD11b/ Mac-1 Monocyte CD33 Ly-71 (F4/80) CD66b Granulocyte CD66b Gr-1/Ly6G Ly6C CD41 CD41 CD61 (Integrin b3) CD61 Platelet CD9 CD62 CD62P (activated platelets) CD235a CD235a Erythrocyte Ter-119 CD146 MECA-32 CD106 CD146 Endothelial Cell CD31 CD62E (activated endothelial cells) Epithelial Cell CD236 CD326 (EPCAM1) For Research Use Only.
T-Cell Antigen CD28 Mediates Adhesion with B Cells by Interacting with Activation Antigen B7/BB-1 PETER S

Proc. Nati. Acad. Sci. USA Vol. 87, pp. 5031-5035, July 1990 Immunology T-cell antigen CD28 mediates adhesion with B cells by interacting with activation antigen B7/BB-1 PETER S. LINSLEY*, EDWARD A. CLARKt, AND JEFFREY A. LEDBETTER* *Oncogen, 3005 First Avenue, Seattle, WA 98121; and tDepartment of Microbiology, University of Washington, Seattle, WA 98195 Communicated by Seymour J. Klebanoff, March 30, 1990 ABSTRACT Studies using monoclonal antibodies (mAbs) intercellular adhesion mediated by major histocompatibility have implicated the homodimeric glycoprotein CD28 as an complex (MHC) class I (13) and class II (14) molecules with important regulator of human T-cell activation, in part by the CD8 and CD4 accessory molecules, respectively. We posttranscriptional control ofcytokine mRNA levels. Although have expressed the CD28 antigen to high levels in Chinese the CD28 antigen has functional and structural characteristics hamster ovary (CHO) cells and have used these transfected of a receptor, a natural ligand for this molecule has not been cells to develop a CD28-mediated cell adhesion assay. By identified. Here we show that the CD28 antigen, expressed in using this assay as a screening method, we have demon- Chinese hamster ovary (CHO) cells, mediated specific inter- strated an interaction between CD28 and a natural ligand cellular adhesion with human lymphoblastoid and leukemic expressed on activated B lymphocytes, the B7/BB-1 antigen. B-cell lines and with activated primary murine B cells. CD28- mediated adhesion was not, dependant upon divalent cations. Several mAbs were identified that inhibited CD28-mediated MATERIALS AND METHODS adhesion, including mAb BB-1 against the B-cell activation mAbs.
Papers J Clin Pathol: First Published As 10.1136/Jcp.49.7.539 on 1 July 1996

Clin Pathol 1996;49:539-544 539 Papers J Clin Pathol: first published as 10.1136/jcp.49.7.539 on 1 July 1996. Downloaded from Differential expression of T cell antigens in normal peripheral blood lymphocytes: a quantitative analysis by flow cytometry L Ginaldi, N Farahat, E Matutes, M De Martinis, R Morilla, D Catovsky Abstract diagnosis by comparison with findings in Aims-To obtain reference values of the normal counterparts. level of expression of T cell antigens on ( Clin Pathol 1996;49:539-544) normal lymphocyte subsets in order to disclose differences which could reflect Keywords: flow cytometry, T cell antigens, peripheral their function or maturation stages, or blood lymphocytes. both. Methods-Peripheral blood from 15 healthy donors was processed by flow The most common use of flow cytometry is to cytometry with triple colour analysis. For determine the percent of "positive" or "nega- each sample phycoerythrin (PE) conju- tive" cells for each antigen in different cell gated CD2, CD4, CD5, CD8, and CD56 populations. However, valuable information is monoclonal antibodies were combined lost when the relative intensities of the positive with Cy5-R-phycoerythrin (TC) conju- cells, reflecting antigenic densities, are not considered. A cell population with a well gated CD3 and fluorescein isothiocyanate http://jcp.bmj.com/ (FITC) conjugated CD7; CD2- and defined phenotype, positive for one antigen, CD7-PE were also combined with might be heterogeneous with regard to its level CD3-TC and CD4-FITC. Standard mi- of expression. This may reflect different crobeads with different capacities to bind functional or maturational states, or both, or mouse immunoglobulins were used to identify subpopulations on the basis of the dif- convert the mean fluorescence intensity ferent numbers of molecules of antigen per cell.
Signaling Expression by IL-7 and TCR Α Receptor Differential Regulation

Differential Regulation of Human IL-7 Receptor α Expression by IL-7 and TCR Signaling This information is current as Nuno L. Alves, Ester M. M. van Leeuwen, Ingrid A. M. of September 24, 2021. Derks and René A. W. van Lier J Immunol 2008; 180:5201-5210; ; doi: 10.4049/jimmunol.180.8.5201 http://www.jimmunol.org/content/180/8/5201 Downloaded from References This article cites 36 articles, 19 of which you can access for free at: http://www.jimmunol.org/content/180/8/5201.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 24, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2008 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Differential Regulation of Human IL-7 Receptor ␣ Expression by IL-7 and TCR Signaling1 Nuno L. Alves,2* Ester M. M. van Leeuwen,3*† Ingrid A. M. Derks,* and Rene´A.
Antibody to CD40 Ligand Inhibits Both Humoral and Cellular Immune Responses to Adenoviral Vectors and Facilitates Repeated Administration to Mouse Airway

Gene Therapy (1997) 4, 611–617 1997 Stockton Press All rights reserved 0969-7128/97 $12.00 Antibody to CD40 ligand inhibits both humoral and cellular immune responses to adenoviral vectors and facilitates repeated administration to mouse airway A Scaria1, JA St George1, RJ Gregory1, RJ Noelle2, SC Wadsworth1, AE Smith1 and JM Kaplan1 1Genzyme Corporation, Framingham, MA; 2Department of Microbiology, Dartmouth Medical School, Lebanon, NH, USA Adenoviral vectors have been used successfully to transfer against murine CD40 ligand inhibits the development of the human CFTR cDNA to respiratory epithelium in animal neutralizing antibodies to adenoviral (Ad) vector. MR1 also models and to CF patients in vivo. However, studies done decreased the cellular immune response to Ad vector and primarily in mice, indicate that present vector systems have allowed an increase in persistence of transgene limitations. Among other things, transgene expression in expression. Furthermore, when administered with a the lung is transient and the production of neutralizing anti- second dose of Ad vector to mice preimmunized against bodies against adenovirus correlates with a reduced ability vector, MR1 was able to interfere with the development of to readminister a vector of the same serotype. Here we a secondary antibody response and allowed for high levels demonstrate that in mice, a transient blockade of costimu- of transgene expression upon a third administration of lation between activated T cells and B cells/antigen vector to the airway. presenting cells
CD18) in a Patient with Leukocyte Adhesion Molecule (Leu-CAM) Deficiency

Point mutations impairing cell surface expression of the common beta subunit (CD18) in a patient with leukocyte adhesion molecule (Leu-CAM) deficiency. M A Arnaout, … , D G Tenen, D M Fathallah J Clin Invest. 1990;85(3):977-981. https://doi.org/10.1172/JCI114529. Research Article The leukocyte adhesion molecules CD11a/CD18, CD11b/CD18, and CD11c/CD18 (Leu-CAM) are members of the integrin receptor family and mediate crucial adhesion-dependent functions in leukocytes. The molecular basis for their deficient cell surface expression was sought in a patient suffering from severe and recurrent bacterial infections. Previous studies revealed that impaired cell surface expression of Leu-CAM is secondary to heterogeneous structural defects in the common beta subunit (CD18). Cloning and sequencing of complementary DNA encoding for CD18 in this patient revealed two mutant alleles, each representing a point mutation in the coding region of CD18 and resulting in an amino acid substitution. Each mutant allele results in impaired CD18 expression on the cell surface membrane of transfected COS M6 cells. One substitution involves an arginine residue (Arg593----cysteine) that is conserved in the highly homologous fourth cysteine-rich repeats of other mammalian integrin subfamilies. The other substitution involves a lysine residue (Lys196----threonine) located within another highly conserved region in integrins. These data identify crucial residues and regions necessary for normal cell surface expression of CD18 and possibly other integrin beta subunits and define a molecular basis for impaired cell surface expression of CD18 in this patient. Find the latest version: https://jci.me/114529/pdf Rapid Publication Point Mutations Impairing Cell Surface Expression of the Common ,B Subunit (CD18) in a Patient with Leukocyte Adhesion Molecule (Leu-CAM) Deficiency M.
CD40-Deficient Mice GEORG A

Proc. Natl. Acad. Sci. USA Vol. 93, pp. 4994-4998, May 1996 Immunology Induction of alloantigen-specific tolerance by B cells from CD40-deficient mice GEORG A. HOLLXNDER*t, EMANUELA CASTIGLIt, ROBERT KULBACKI§, MICHAEL SU*, STEVEN J. BURAKOFF*, JOSEI-CARLOS GUTIERREZ-RAMOS§, AND RAIF S. GEHAt *Division of Pediatric Oncology, Dana-Farber Cancer Institute, Department of Pediatrics, tDivision of Immunology, The Children's Hospital, Department of Pediatrics, §Center for Blood Research, Harvard Medical School, Boston, MA 02115 Communicated by Frederick W Alt, The Children's Hospital, Boston, MA, January 22, 1996 (received for review November 17, 1995) ABSTRACT Interaction between CD40 on B cells and The capacity of B cells to provide ligands for T-cell specific CD40 ligand molecules on T cells is pivotal for the generation costimulatory molecules determines the outcome of T-cell of a thymus-dependent antibody response. Here we show that activation. Resting B cells express only limited amounts of B cells deficient in CD40 expression are unable to elicit the costimulatory molecules compared to activated B cells (11) proliferation of allogeneic T cells in vitro. More importantly, and are thus ineffective as antigen presenting cells (12). This mice immunized with CD40-1- B cells become tolerant to concept has also been demonstrated in vivo. For instance, allogeneic major histocompatibility complex (MHC) antigens monovalent rabbit anti-mouse IgD when presented by small as measured by a mixed lymphocyte reaction and cytotoxic resting B cells rendered mice tolerant to rabbit Ig (13). T-cell assay. The failure of CD40-'- B cells to serve as antigen Polyclonal activation of antigen presenting B cells (e.g., by presenting cells in vitro was corrected by the addition of crosslinking with divalent rabbit anti-mouse IgD) prevented anti-CD28 mAb.
Inflammatory Lesions (CD80) and B7.2 (CD86) in Vitro and In

Human Muscle Cells Express a Functional Costimulatory Molecule Distinct from B7.1 (CD80) and B7.2 (CD86) In Vitro and in Inflammatory Lesions This information is current as of September 26, 2021. Lüder Behrens, Martin Kerschensteiner, Thomas Misgeld, Norbert Goebels, Hartmut Wekerle and Reinhard Hohlfeld J Immunol 1998; 161:5943-5951; ; http://www.jimmunol.org/content/161/11/5943 Downloaded from References This article cites 49 articles, 19 of which you can access for free at: http://www.jimmunol.org/content/161/11/5943.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 26, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 1998 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Human Muscle Cells Express a Functional Costimulatory Molecule Distinct from B7.1 (CD80) and B7.2 (CD86) In Vitro and in Inﬂammatory Lesions1 Lu¨der Behrens,* Martin Kerschensteiner,* Thomas Misgeld,* Norbert Goebels,*† Hartmut Wekerle,* and Reinhard Hohlfeld2*† The B7 family of costimulatory molecules likely includes members distinct from B7.1 (CD80) and B7.2 (CD86).
Immunomodulation by Thalidomide and Thalidomide Analogues

Ann Rheum Dis 1999;58:(Suppl I) I107–I113 I107 Ann Rheum Dis: first published as 10.1136/ard.58.2008.i107 on 1 November 1999. Downloaded from Immunomodulation by thalidomide and thalidomide analogues Laura G Corral, Gilla Kaplan Tumour necrosis factor á (TNFá), a key stimulate the anti-inﬂammatory cytokine IL10. cytokine involved in the host immune re- Similarly to thalidomide, these drugs that do sponse, also contributes to the pathogenesis of not inhibit PDE4 act as costimulators of T cells both infectious and autoimmune diseases. To but are much more potent than the parent ameliorate the pathology resulting from TNFá drug. The distinct immunomodulatory activity in these clinical settings, strategies for the inhi- of these new TNFá inhibitors may potentially bition of this cytokine have been developed. allow them to be used in the clinic for the Our previous work has shown that the drug treatment of a wide variety of immunopatho- thalidomide is a partial inhibitor of TNFá pro- logical disorders of diVerent aetiologies. duction in vivo. For example, when leprosy patients suVering from erythema nodosum TNFá is a key player in the immune leprosum (ENL) are treated with thalidomide, response the increased serum TNFá concentrations TNFá is a pleiotropic cytokine produced characteristic of this syndrome are reduced, primarily by monocytes and macrophages, but with a concomitant improvement in clinical also by lymphocytes and NK cells. TNFá plays symptoms. Similarly, we have found that in a central part in the host immune response to patients with tuberculosis, with or without HIV viral, parasitic, fungal and bacterial infections.
The Immunological Synapse and CD28-CD80 Interactions Shannon K

© 2001 Nature Publishing Group http://immunol.nature.com ARTICLES The immunological synapse and CD28-CD80 interactions Shannon K. Bromley1,Andrea Iaboni2, Simon J. Davis2,Adrian Whitty3, Jonathan M. Green4, Andrey S. Shaw1,ArthurWeiss5 and Michael L. Dustin5,6 Published online: 19 November 2001, DOI: 10.1038/ni737 According to the two-signal model of T cell activation, costimulatory molecules augment T cell receptor (TCR) signaling, whereas adhesion molecules enhance TCR–MHC-peptide recognition.The structure and binding properties of CD28 imply that it may perform both functions, blurring the distinction between adhesion and costimulatory molecules. Our results show that CD28 on naïve T cells does not support adhesion and has little or no capacity for directly enhancing TCR–MHC- peptide interactions. Instead of being dependent on costimulatory signaling, we propose that a key function of the immunological synapse is to generate a cellular microenvironment that favors the interactions of potent secondary signaling molecules, such as CD28. The T cell receptor (TCR) interaction with complexes of peptide and as CD2 and CD48, which suggests that CD28 might have a dual role as major histocompatibility complex (pMHC) is central to the T cell an adhesion and a signaling molecule4. Coengagement of CD28 with response. However, efficient T cell activation also requires the partici- the TCR has a number of effects on T cell activation; these include pation of additional cell-surface receptors that engage nonpolymorphic increasing sensitivity to TCR stimulation and increasing the survival of ligands on antigen-presenting cells (APCs). Some of these molecules T cells after stimulation5. CD80-transfected APCs have been used to are involved in the “physical embrace” between T cells and APCs and assess the temporal relationship of TCR and CD28 signaling, as initiat- are characterized as adhesion molecules.
Iotest CD86 (B7-2)-PC7

IOTest CD86 (B7-2)-PC7 PN B30648 – 0.5 mL – Liquid – Clone HA5.2B7 Analyte Specific Reagent. Analytical and performance characteristics are not established. SPECIFICITY REAGENT CONTENTS SELECTED RESEARCH REFERENCES The anti-human HA5.2B7 monoclonal This antibody is provided in phosphate- 1. Rennert, P., Furlong, K., Jellis, C., antibody (mAb) binds specifically to CD86 buffered saline, containing 0.1% sodium Greenfield, E., Freeman, G.J., Ueda, Y, (B7-2) antigen (1). azide and 2 mg/mL bovine serum albumin. Levine, B., June, C.H. and Gray, G.S. The CD86 antigen (B7-2, B70) is a single Concentration: See lot specific Certificate of “The IgV domain of human B7-2 chain transmembrane glycoprotein, Analysis at www.beckmancoulter.com. (CD86) is sufficient to co-stimulate T structurally similar to CD80 (B7-1) (2, 3). Its lymphocytes and induce cytokine molecular weight is 80 kDa, under reducing STATEMENTS OF WARNING secretion”, International Immunology, conditions. The extracellular region is 1. This reagent contains 0.1% sodium 1997, 9, 6, 805–813. composed of one V-type and one C-type Ig- azide. Sodium azide under acid 2. Boussiotis, V.A., Freeman, G.J., like domains. There are 8 potential sites for conditions yields hydrazoic acid, an Gribben, J.G., Daley, J., Gray, G., N-glycosylation. The cytoplasmic tail has 3 extremely toxic compound. Azide Nadler, L.M., "Activated human B potential sites for protein kinase C compounds should be flushed with lymphocytes express three CTLA-4 phosphorylation (4, 5). CD86 shares with running water while being discarded. counterreceptors that costimulate T-cell CD80 the same co-receptors on T cells, These precautions are recommended activation", 1993, Proc.
Cells Expressing Truncated Major Histocompatibility Complex

Proc. Natl. Acad. Sci. USA Vol. 90, pp. 5687-5690, June 1993 Immunology Constitutive expression of B7 restores immunogenicity of tumor cells expressing truncated major histocompatibility complex class II molecules (CD28/tumor immunity) SIVASUBRAMANIAN BASKAR*, SUZANNE OSTRAND-ROSENBERG*t, NASRIN NABAVIt, LEE M. NADLER§, GORDON J. FREEMAN§, AND LAURIE H. GLIMCHER¶ *Department of Biological Sciences, University of Maryland, Baltimore, MD 21228; *Department of Immunopharmacology, Roche Research Center, Nutley, NJ 07110-1199; §Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115; and lDepartment of Cancer Biology, Harvard School of Public Health, and Department of Medicine, Harvard Medical School, Boston, MA 02115 Communicated by Leroy Hood, March 12, 1993 ABSTRACT The inability of the autologous host to reject B7 coactivation signal. Immunization with such engineered resident tumor cells is frequently the result of inadequate tumor cells generates potent tumor-specific CD4+ T cells that generation of tumor-specific T cells. Specific activation of T facilitate rejection and confer immunologic memory to high- cells occurs after delivery of two signals by the antigen- dose challenges of wild-type neoplastic cells. These results presenting cell. The first signal is antigen-specific and is the demonstrate the critical role ofthe B7 costimulatory pathway engagement of the T-cell antigen receptor by a specific major in stimulating tumor-specific CD4+ T cells and provide an histocompatiblity complex antigen-peptide complex. For some attractive strategy for enhancing tumor immunity. T cells, the second or costimulatory signal is the interaction of the T-cell CD28 receptor with the B7 activation molecule of the antigen-presenting cell.